ID MMP2_MOUSE Reviewed; 662 AA. AC P33434; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 27-MAR-2024, entry version 203. DE RecName: Full=72 kDa type IV collagenase; DE EC=3.4.24.24 {ECO:0000250|UniProtKB:P08253}; DE AltName: Full=72 kDa gelatinase; DE AltName: Full=Gelatinase A; DE AltName: Full=Matrix metalloproteinase-2; DE Short=MMP-2; DE Contains: DE RecName: Full=PEX; DE Flags: Precursor; GN Name=Mmp2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1373140; DOI=10.1016/s0021-9258(18)42592-6; RA Reponen P., Sahlberg C., Huhtala P., Hurskainen T., Thesleff I., RA Tryggvason K.; RT "Molecular cloning of murine 72-kDa type IV collagenase and its expression RT during mouse development."; RL J. Biol. Chem. 267:7856-7862(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX PubMed=2744464; DOI=10.1101/gad.3.6.848; RA Brenner C.A., Adler R.R., Rappolee D.A., Pedersen R.A., Werb Z.; RT "Genes for extracellular-matrix-degrading metalloproteinases and their RT inhibitor, TIMP, are expressed during early mammalian development."; RL Genes Dev. 3:848-859(1989). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Lung; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [5] RP ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22509276; DOI=10.1371/journal.pone.0034177; RA Lovett D.H., Mahimkar R., Raffai R.L., Cape L., Maklashina E., Cecchini G., RA Karliner J.S.; RT "A novel intracellular isoform of matrix metalloproteinase-2 induced by RT oxidative stress activates innate immunity."; RL PLoS ONE 7:E34177-E34177(2012). CC -!- FUNCTION: Ubiquitinous metalloproteinase that is involved in diverse CC functions such as remodeling of the vasculature, angiogenesis, tissue CC repair, tumor invasion, inflammation, and atherosclerotic plaque CC rupture. As well as degrading extracellular matrix proteins, can also CC act on several nonmatrix proteins such as big endothelial 1 and beta- CC type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu CC bond. Appears to have a role in myocardial cell death pathways. CC Contributes to myocardial oxidative stress by regulating the activity CC of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of CC the fibrovascular tissues (By similarity). {ECO:0000250}. CC -!- FUNCTION: PEX, the C-terminal non-catalytic fragment of MMP2, posseses CC anti-angiogenic and anti-tumor properties and inhibits cell migration CC and cell adhesion to FGF2 and vitronectin. Ligand for integrin alpha- CC v/beta-3 on the surface of blood vessels (By similarity). CC {ECO:0000250}. CC -!- FUNCTION: [Isoform 2]: Mediates the proteolysis of CHUK/IKKA and CC initiates a primary innate immune response by inducing mitochondrial- CC nuclear stress signaling with activation of the pro-inflammatory NF- CC kappaB, NFAT and IRF transcriptional pathways. CC {ECO:0000269|PubMed:22509276}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Cleavage of gelatin type I and collagen types IV, V, VII, X. CC Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.; CC EC=3.4.24.24; Evidence={ECO:0000250|UniProtKB:P08253}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000250|UniProtKB:P08253}; CC Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:P08253}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P08253}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P08253}; CC -!- SUBUNIT: Interacts (via the C-terminal hemopexin-like domains- CC containing region) with the integrin alpha-V/beta-3; the interaction CC promotes vascular invasion in angiogenic vessels and melamoma cells. CC Interacts (via the C-terminal PEX domain) with TIMP2 (via the C- CC terminal); the interaction inhibits the degradation activity. Interacts CC with GSK3B (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted, extracellular space, CC extracellular matrix {ECO:0000250}. Membrane {ECO:0000250}. Nucleus CC {ECO:0000250}. Note=Colocalizes with integrin alphaV/beta3 at the CC membrane surface in angiogenic blood vessels and melanomas. Found in CC mitochondria, along microfibrils, and in nuclei of cardiomyocytes (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Mitochondrion. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P33434-1; Sequence=Displayed; CC Name=2; CC IsoId=P33434-2; Sequence=VSP_044632; CC -!- DEVELOPMENTAL STAGE: Present in unfertilized eggs and at the zygote and CC cleavage stages. Levels increase at the blastocyst stage and with CC endoderm differentiation. {ECO:0000269|PubMed:2744464}. CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif CC binds the catalytic zinc ion, thus inhibiting the enzyme. The CC dissociation of the cysteine from the zinc ion upon the activation- CC peptide release activates the enzyme. CC -!- PTM: Phosphorylation on multiple sites modulates enzymatic activity. CC Phosphorylated by PKC in vitro (By similarity). {ECO:0000250}. CC -!- PTM: The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3) CC (By similarity). Autocatalytic cleavage in the C-terminal produces the CC anti-angiogenic peptide, PEX. This processing appears to be facilitated CC by binding integrinv/beta3 (By similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform 2]: Induced by oxidative stress. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M84324; AAA39338.1; -; mRNA. DR EMBL; BC070430; AAH70430.1; -; mRNA. DR CCDS; CCDS22523.1; -. [P33434-1] DR PIR; A42496; A42496. DR RefSeq; NP_032636.1; NM_008610.3. [P33434-1] DR AlphaFoldDB; P33434; -. DR SMR; P33434; -. DR BioGRID; 201449; 16. DR IntAct; P33434; 1. DR STRING; 10090.ENSMUSP00000034187; -. DR BindingDB; P33434; -. DR ChEMBL; CHEMBL3095; -. DR MEROPS; M10.003; -. DR GlyCosmos; P33434; 2 sites, No reported glycans. DR GlyGen; P33434; 2 sites. DR PhosphoSitePlus; P33434; -. DR CPTAC; non-CPTAC-3729; -. DR MaxQB; P33434; -. DR PaxDb; 10090-ENSMUSP00000034187; -. DR PeptideAtlas; P33434; -. DR ProteomicsDB; 295691; -. [P33434-1] DR ProteomicsDB; 295692; -. [P33434-2] DR Pumba; P33434; -. DR ABCD; P33434; 1 sequenced antibody. DR Antibodypedia; 773; 1942 antibodies from 52 providers. DR DNASU; 17390; -. DR Ensembl; ENSMUST00000034187.9; ENSMUSP00000034187.8; ENSMUSG00000031740.9. [P33434-1] DR GeneID; 17390; -. DR KEGG; mmu:17390; -. DR UCSC; uc009mue.1; mouse. [P33434-1] DR AGR; MGI:97009; -. DR CTD; 4313; -. DR MGI; MGI:97009; Mmp2. DR VEuPathDB; HostDB:ENSMUSG00000031740; -. DR eggNOG; KOG1565; Eukaryota. DR GeneTree; ENSGT00940000158511; -. DR HOGENOM; CLU_015489_6_2_1; -. DR InParanoid; P33434; -. DR OMA; CPKDSCN; -. DR OrthoDB; 5340816at2759; -. DR PhylomeDB; P33434; -. DR TreeFam; TF315428; -. DR BRENDA; 3.4.24.24; 3474. DR Reactome; R-MMU-1442490; Collagen degradation. DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix. DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases. DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells. DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling. DR BioGRID-ORCS; 17390; 4 hits in 76 CRISPR screens. DR ChiTaRS; Mmp2; mouse. DR PRO; PR:P33434; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; P33434; Protein. DR Bgee; ENSMUSG00000031740; Expressed in epithelium of cochlear duct and 245 other cell types or tissues. DR ExpressionAtlas; P33434; baseline and differential. DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro. DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0030017; C:sarcomere; IDA:MGI. DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI. DR GO; GO:0001968; F:fibronectin binding; ISO:MGI. DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:MGI. DR GO; GO:0008237; F:metallopeptidase activity; ISO:MGI. DR GO; GO:0008233; F:peptidase activity; ISO:MGI. DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0001955; P:blood vessel maturation; IGI:MGI. DR GO; GO:0060346; P:bone trabecula formation; IGI:MGI. DR GO; GO:0016477; P:cell migration; ISO:MGI. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI. DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:MGI. DR GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl. DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl. DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:MGI. DR GO; GO:0071492; P:cellular response to UV-A; ISS:UniProtKB. DR GO; GO:0030574; P:collagen catabolic process; IMP:MGI. DR GO; GO:0007566; P:embryo implantation; IDA:MGI. DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0060325; P:face morphogenesis; IGI:MGI. DR GO; GO:0007507; P:heart development; ISO:MGI. DR GO; GO:0001957; P:intramembranous ossification; IGI:MGI. DR GO; GO:0001553; P:luteinization; IEA:Ensembl. DR GO; GO:0048246; P:macrophage chemotaxis; ISO:MGI. DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI. DR GO; GO:0045906; P:negative regulation of vasoconstriction; ISO:MGI. DR GO; GO:0001541; P:ovarian follicle development; ISO:MGI. DR GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl. DR GO; GO:0007567; P:parturition; IEA:Ensembl. DR GO; GO:0014012; P:peripheral nervous system axon regeneration; ISO:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI. DR GO; GO:1903378; P:positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISO:MGI. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:MGI. DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI. DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; ISO:MGI. DR GO; GO:0030163; P:protein catabolic process; ISO:MGI. DR GO; GO:0006508; P:proteolysis; ISO:MGI. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:1904645; P:response to amyloid-beta; IDA:ARUK-UCL. DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl. DR GO; GO:0043627; P:response to estrogen; ISO:MGI. DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI. DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IDA:MGI. DR GO; GO:0009612; P:response to mechanical stimulus; ISO:MGI. DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI. DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI. DR GO; GO:0048705; P:skeletal system morphogenesis; IGI:MGI. DR GO; GO:0048771; P:tissue remodeling; ISO:MGI. DR CDD; cd00062; FN2; 3. DR CDD; cd00094; HX; 1. DR CDD; cd04278; ZnMc_MMP; 1. DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 2. DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 2. DR Gene3D; 2.110.10.10; Hemopexin-like domain; 1. DR InterPro; IPR000562; FN_type2_dom. DR InterPro; IPR036943; FN_type2_sf. DR InterPro; IPR000585; Hemopexin-like_dom. DR InterPro; IPR036375; Hemopexin-like_dom_sf. DR InterPro; IPR018487; Hemopexin-like_repeat. DR InterPro; IPR018486; Hemopexin_CS. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR033739; M10A_MMP. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001818; Pept_M10_metallopeptidase. DR InterPro; IPR021190; Pept_M10A. DR InterPro; IPR021158; Pept_M10A_Zn_BS. DR InterPro; IPR006026; Peptidase_Metallo. DR InterPro; IPR036365; PGBD-like_sf. DR PANTHER; PTHR10201:SF29; 72 KDA TYPE IV COLLAGENASE; 1. DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1. DR Pfam; PF00040; fn2; 3. DR Pfam; PF00045; Hemopexin; 4. DR Pfam; PF00413; Peptidase_M10; 2. DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1. DR PRINTS; PR00013; FNTYPEII. DR PRINTS; PR00138; MATRIXIN. DR SMART; SM00059; FN2; 3. DR SMART; SM00120; HX; 4. DR SMART; SM00235; ZnMc; 1. DR SUPFAM; SSF50923; Hemopexin-like domain; 1. DR SUPFAM; SSF57440; Kringle-like; 3. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR SUPFAM; SSF47090; PGBD-like; 1. DR PROSITE; PS00546; CYSTEINE_SWITCH; 1. DR PROSITE; PS00023; FN2_1; 3. DR PROSITE; PS51092; FN2_2; 3. DR PROSITE; PS00024; HEMOPEXIN; 1. DR PROSITE; PS51642; HEMOPEXIN_2; 4. DR PROSITE; PS00142; ZINC_PROTEASE; 1. DR Genevisible; P33434; MM. PE 1: Evidence at protein level; KW Alternative splicing; Angiogenesis; Autocatalytic cleavage; Calcium; KW Collagen degradation; Cytoplasm; Disulfide bond; Extracellular matrix; KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; KW Mitochondrion; Nucleus; Phosphoprotein; Protease; Reference proteome; KW Repeat; Secreted; Signal; Zinc; Zymogen. FT SIGNAL 1..29 FT /evidence="ECO:0000250|UniProtKB:P33436" FT PROPEP 30..109 FT /note="Activation peptide" FT /id="PRO_0000028716" FT CHAIN 110..662 FT /note="72 kDa type IV collagenase" FT /id="PRO_0000028717" FT CHAIN 445..662 FT /note="PEX" FT /evidence="ECO:0000250" FT /id="PRO_0000391627" FT DOMAIN 228..276 FT /note="Fibronectin type-II 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DOMAIN 286..334 FT /note="Fibronectin type-II 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DOMAIN 344..392 FT /note="Fibronectin type-II 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT REPEAT 474..518 FT /note="Hemopexin 1" FT REPEAT 519..565 FT /note="Hemopexin 2" FT REPEAT 567..615 FT /note="Hemopexin 3" FT REPEAT 616..662 FT /note="Hemopexin 4" FT REGION 110..221 FT /note="Collagenase-like 1" FT REGION 222..396 FT /note="Collagen-binding" FT REGION 397..467 FT /note="Collagenase-like 2" FT REGION 414..662 FT /note="Required for inhibitor TIMP2 binding" FT /evidence="ECO:0000250" FT REGION 446..465 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 100..107 FT /note="Cysteine switch" FT /evidence="ECO:0000250" FT ACT_SITE 404 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 102 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /note="in inhibited form" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 134 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 168 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 178 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 180 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 185 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 186 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 193 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 200 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 202 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 204 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 206 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 208 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 209 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 211 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 211 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 403 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 407 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 413 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 478 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 523 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 571 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P08253" FT BINDING 620 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P08253" FT CARBOHYD 575 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 644 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 233..259 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DISULFID 247..274 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DISULFID 291..317 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DISULFID 305..332 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DISULFID 349..375 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DISULFID 363..390 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DISULFID 471..662 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT VAR_SEQ 1..76 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_044632" SQ SEQUENCE 662 AA; 74102 MW; C630A7DBDB272F02 CRC64; MEARVAWGAL AGPLRVLCVL CCLLGRAIAA PSPIIKFPGD VAPKTDKELA VQYLNTFYGC PKESCNLFVL KDTLKKMQKF FGLPQTGDLD QNTIETMRKP RCGNPDVANY NFFPRKPKWD KNQITYRIIG YTPDLDPETV DDAFARALKV WSDVTPLRFS RIHDGEADIM INFGRWEHGD GYPFDGKDGL LAHAFAPGTG VGGDSHFDDD ELWTLGEGQV VRVKYGNADG EYCKFPFLFN GREYSSCTDT GRSDGFLWCS TTYNFEKDGK YGFCPHEALF TMGGNADGQP CKFPFRFQGT SYNSCTTEGR TDGYRWCGTT EDYDRDKKYG FCPETAMSTV GGNSEGAPCV FPFTFLGNKY ESCTSAGRND GKVWCATTTN YDDDRKWGFC PDQGYSLFLV AAHEFGHAMG LEHSQDPGAL MAPIYTYTKN FRLSHDDIKG IQELYGPSPD ADTDTGTGPT PTLGPVTPEI CKQDIVFDGI AQIRGEIFFF KDRFIWRTVT PRDKPTGPLL VATFWPELPE KIDAVYEAPQ EEKAVFFAGN EYWVYSASTL ERGYPKPLTS LGLPPDVQQV DAAFNWSKNK KTYIFAGDKF WRYNEVKKKM DPGFPKLIAD SWNAIPDNLD AVVDLQGGGH SYFFKGAYYL KLENQSLKSV KFGSIKSDWL GC //